Rapid and sensitive method to detect oxidized forms of rhGCSF using agilent 2100 bioanalyzer

Analytical Letters

Volumn 42, Issue 8, 2009, Pages 1070-1083

  Somani, Sandeep ^a   Mandal, Goutam ^a   Banerjee, Sampali ^a   Prasad, Ketaki Sabnis ^a   Padmanabhan, Sriram ^a  

^a LUPIN LIMITED   (India)

Author keywords

Bioanalyzer; GCSF; Hydrogen peroxide; NFS 60 cell proliferation assay; Oxidation

Indexed keywords

EID: 70349817545     PISSN: 00032719     EISSN: 1532236X     Source Type: Journal    
DOI: 10.1080/00032710902890454     Document Type: Article

References (33)

1. Brena, R.M., Auer, H., Kornacker, K., Hackanson, B., Raval, A., Byrd, J.C., and Plass, C. 2006. Accurate quantification of DNA methylation using combined bisulfite restriction analysis coupled with the Agilent 2100 bioanalyzer platform. Nucleic Acids Res., 34: e17.
2. Brot, N. and Weissbach, H.1983. Biochemistry and physiological role of methionine sulfoxide residues in proteins. Arch. Biochem. Biophys.,223: 271-281.
3. DalleDonne, I., Milzani, A., and Colombo, R. 1999. The tert-butyl hydroperoxide-induced oxidation of actin Cys-374 is coupled with structural changes in distant regions of the protein. Biochemistry, 38: 12471-12480.
4. Duenas, E.T., Keck, R., Vos, D., Jones, A.S., and Cleland, J.L. 2001. Comparison between light induced and chemically induced oxidation of rhVEGF. Pharm. Res., 18: 1455-1460.
5. Gao, J., Yin, D.H., Yao, Y., Williams, T.D., and Squier, T.C. 1998a. Progressive decline in the ability of calmodulin isolated from aged brain to activate the plasma membrane Ca-ATPase. Biochemistry, 37: 9536-9548.
6. Gao, J., Yin, D.H., Yao, Y., Sun, H., Qin, Z., Schöneich, C., Williams, T.D., and Squier, T.C. 1998b. Loss of conformational stability in calmodulin upon methionine oxidation. Biophys. J., 74: 1115-1134.
7. Gottwald, E., Müller, O., and Polten, A. 2001. Semiquantitative reverse transcription-polymerase chain reaction with the Agilent2100bioanalyzer. Electrophoresis, 22: 4016-4022.
8. Halliwell, B. and Gutteridge, J.M.C. 1999. Free Radicals in Biology and Medicine, 3rd ed. New York: Oxford University Press.
9. Hoshi, T. and Heinemann, S.H. 2001. Regulation of cell function by methionine oxidation and reduction. J. Physiol., 531: 1-11.
10. Houghten, R.A. and Li, C.H. 1983. Reduction of sulfoxides in peptides and proteins. Methods Enzymol., 91: 549-559.
11. Keck, R.G. 1996. The use of t-butyl hydroperoxide as a probe for methionine oxidation in proteins. Anal. Biochem., 236: 56-62.
12. Kim, Y.H., Berry, A.H., Spencer, D.S., and Stites, W.E. 2001. Comparing the effect on protein stability of methionine oxidation versus mutagenesis: Steps toward engineering oxidative resistance in proteins. Protein Eng., 14: 343-347.
13. Levine, R.L., Mosoni, L., Berlett, B.S., and Stadtman, E.R. 1996. Methionine residues as endogenous antioxidants in proteins. Proc. Natl. Acad. Sci. USA, 93: 15036-15040.
14. Li, S., Schöneich, C., and Borchardt, R.T. 1995. Chemical instability of protein pharmaceuticals: Mechanisms of oxidation and strategies for stabilization. Biotechnol. Bioeng., 48: 490-500.
15. Lischwe, M.A. and Sung, M.T. 1977. Use of chlorosuccinamide=urea for the selective cleavage of tryptophanyl peptide bonds in proteins. J. Biol. Chem., 252: 4976-4980.
16. Liu, J.L., Lu, K.V., Eris, T., Katta, V., Westkott, K.R., Narhi, L.O., and Lu, H.S. 1998. In vitro methionine oxidation of recombinant human leptin. Pharm. Res., 15: 632-640.
17. Lu, H.S., Fausset, P.R., Narhi, L.O., Horan, T., Shinagawa, K., Shimamoto, G., and Boone, T.C. 1999. Chemical modification and site-directed mutagenesis of methionine residues in recombinant human granulocyte colony-stimulating factor: Effect on stability and biological activity. Arch. Biochem. Biophys., 362: 1-11.
18. Maas, C., Hermeling, S., Bouma, B., Jiskoot, W., and Gebbink, M.F. 2007. A role for protein misfolding in immunogenicity of biopharmaceuticals. J. Biol. Chem., 282: 2229-2236.
19. Mussa, N.A., Cheung, K.Y., Alam, I.M., and Flatman, S. 2000. The application of the 2100 bioanalyzer-protein chip in the biotechnology industry. Available at http://www.lonza.com/group/en/company/news/publications.
20. Nabuchi, Y., Fujiwara, E., Ueno, K., Kuboniwa, H., Asoh, Y., and Ushio, H. 1995. Oxidation of recombinant human parathyroid hormone: Effect of oxidized position on the biological activity. Pharmacol. Res., 12: 2049-2052.
21. Pavlou, A.K. and Reichert, J.M. 2004. Recombinant protein therapeutics: Success rates, market trends, and values to 2010. Nat. Biotech., 22: 1513-1519.
22. Reubsaet, J.L., Beijnen, J.H., Bult, A., Hop, E., Scholten, S.D., Teeuwsen, J., and Underberg, W.J. 1998. Oxidation of recombinant methionyl human granulocyte colony stimulating factor. J. Pharm. Biomed. Anal., 17: 283-289.
23. Shirafuji, N., Asano, S., Matsuda, S., Watari, K., Takaku, F., and Nagata, S. 1989. A new bioassay for human granulocyte colony-stimulating factor (hG-CSF) using murine myeloblastic NFS-60 cells as targets and estimation of its levels in sera from normal healthy persons and patients with infectious and hematological disorders. Exp. Hematol., 17: 116-119.
24. Skufca, P., Seibert, F., and Grimm, R. 2008. Stable aqueous G-CSF containing compositions. U.S. Patent Application 20080026046.
25. Sodowich, B.I., Fadl, I., and Burns, C. 2007. Method validation of in vitro RNA transcript analysis on the Agilent 2100 bioanalyzer. Electrophoresis, 28: 2368-2378.
26. Stadtman, E.R. 1992. Protein oxidation and aging. Science., 257: 1220-1224.
27. Tsuchiya, M., Nomura, H., Asano, S., Kaziro, Y., and Nagata, S. 1987. Characterization of recombinant human granulocyte-colony-stimulating factor produced in mouse cells. EMBO J., 6: 611-616.
28. Underberg, W.J., Hoitink, M.A., Reubsaet, J.L., and Waterval, J.C. 2000. Separation and detection techniques for peptides and proteins in stability research and bioanalysis. J. Chromatogr. B, 742: 401-409.
29. Van Patten, S.M.V., Hanson, E., Bernasconi, R., Zhang, K., Manavalan, P., Cole, E.S., McPherson, J.M., and Edmunds, T. 1999. Oxidation of methionine residues in antithrombin: Effects on biological activity and heparin binding. J. Biol. Chem., 274: 10268-10276.
30. Vanz, A.L.S., Renard, G., Palma, M.S., Chies, J.M., Dalmora, S.L., Basso, L.A., and Santos, D.S. 2008. Human granulocyte colony stimulating factor (hG-CSF): Cloning, overexpression, purification, and characterization. Microb. Cell Fact., 7: 1-12.
31. Volkin, D.B., Mach, H., and Middaugh, C.R. 1997. Degradative covalent reactions important to protein stability. Mol. Biotechnol., 8: 105-122.
32. Whitelegge, J.P., Penn, B., To, T., Johnson, J., Waring, A., Sherman, M., Stevens, R.L., Fluharty, C.B., Faull, K.F., and Flauharty, A.L. 2000. Methionine oxidation within the cerebroside-sulfate activator protein (CSAct or Saposin B). Protein Sci., 9: 1618-1630.
33. Yin, J., Chu, J.W., Ricci, M.S., Brems, D.N., Wang, D.I.C., and Trout, B.L. 2005. Effects of excipients on the hydrogen peroxide-induced oxidation of methionine residues in granulocyte colony-stimulating factor. Pharmacol. Res., 22: 141-147.